CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015502
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase Arkadia 
Protein Synonyms/Alias
 RING finger protein 111 
Gene Name
 RNF111 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
34PKTQESLKGILLHPEubiquitination[1]
87GNQQEQEKSLVVRKKubiquitination[1]
173SQTILNAKSRSHSARubiquitination[1]
932TDWFSQRKLHCKQDGubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 Acts in the NODAL pathway of mesoderm patterning during embryonic development. Acts downstream AXIN1 as an E3 ubiquitin- protein ligase which promotes the ubiquitination of inhibitory SMADs such as SMAD7, induces their proteasomal degradation and thereby enhances the transcriptional activity of TGF-beta and BMP. Activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation. 
Sequence Annotation
 ZN_FING 942 983 RING-type; atypical.
 REGION 241 404 Interaction with AXIN1.
 MOTIF 300 304 SUMO interaction motif 1 (SIM); mediates
 MOTIF 325 331 SUMO interaction motif 2 (SIM); mediates
 MOTIF 382 386 SUMO interaction motif 3 (SIM); mediates  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Developmental protein; Ligase; Metal-binding; Nucleus; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 994 AA 
Protein Sequence
MSQWTPEYNE LYTLKVDMKS EIPSDAPKTQ ESLKGILLHP EPIGAAKSFP AGVEMINSKV 60
GNEFSHLCDD SQKQEKEMNG NQQEQEKSLV VRKKRKSQQA GPSYVQNCVK ENQGILGLRQ 120
HLGTPSDEDN DSSFSDCLSS PSSSLHFGDS DTVTSDEDKE VSVRHSQTIL NAKSRSHSAR 180
SHKWPRTETE SVSGLLMKRP CLHGSSLRRL PCRKRFVKNN SSQRTQKQKE RILMQRKKRE 240
VLARRKYALL PSSSSSSEND LSSESSSSSS TEGEEDLFVS ASENHQNNPA VPSGSIDEDV 300
VVIEASSTPQ VTANEEINVT STDSEVEIVT VGESYRSRST LGHSRSHWSQ GSSSHASRPQ 360
EPRNRSRIST VIQPLRQNAA EVVDLTVDED EPTVVPTTSA RMESQATSAS INNSNPSTSE 420
QASDTASAVT SSQPSTVSET SATLTSNSTT GTSIGDDSRR TTSSAVTETG PPAMPRLPSC 480
CPQHSPCGGS SQNHHALGHP HTSCFQQHGH HFQHHHHHHH TPHPAVPVSP SFSDPACPVE 540
RPPQVQAPCG ANSSSGTSYH EQQALPVDLS NSGIRSHGSG SFHGASAFDP CCPVSSSRAA 600
IFGHQAAAAA PSQPLSSIDG YGSSMVAQPQ PQPPPQPSLS SCRHYMPPPY ASLTRPLHHQ 660
ASACPHSHGN PPPQTQPPPQ VDYVIPHPVH AFHSQISSHA TSHPVAPPPP THLASTAAPI 720
PQHLPPTHQP ISHHIPATAP PAQRLHPHEV MQRMEVQRRR MMQHPTGLFV FCVSRRAHER 780
PPPHPHRMHP NYGHGHHIHV PQTMSSHPRQ APERSAWELG IEAGVTAATY TPGALHPHLA 840
HYHAPPRLHH LQLGALPLMV PDMAGYPHIR YISSGLDGTS FRGPFRGNFE ELIHLEERLG 900
NVNRGASQGT IERCTYPHKY KKVTTDWFSQ RKLHCKQDGE EGTEEDTEEK CTICLSILEE 960
GEDVRRLPCM HLFHQVCVDQ WLITNKKCPI CRVDIEAQLP SES 1003 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0032184; F:SUMO polymer binding; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IMP:BHF-UCL.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007389; P:pattern specification process; IEA:Compara.
 GO:0031398; P:positive regulation of protein ubiquitination; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
 GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Compara.
 GO:0000209; P:protein polyubiquitination; IEA:Compara.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; IEA:Compara. 
Interpro
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS